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Microbiology 142 (1996), 2567-2576
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microbiology, Vol 142, 2567-2576, Copyright © 1996 by Society for General Microbiology

ARTICLES

An extracellular enzyme with hyaluronidase and chondroitinase activities from some oral anaerobic spirochaetes

D Scott, R Siboo, EC Chan and R Siboo
Department of Microbiology and Immunology, Faculty of Medicine, McGill University, Montreal, Quebec, Canada.

Treponema denticola, Treponema vincentii and Treponema socranskii produce an enzyme that hydrolyses hyaluronic acid (HA) and chondroitin sulphate (CS). The secreted enzyme is specifically inhibited by gold sodium thiomalate and anti-bee-venom antibodies. The use of saturated substrate (HA or CS) transblots allowed the visualization of active enzyme directly from culture supernatants and is a useful tool in clarification of complex polysaccharide-degrading enzyme specificities. The affinity-purified extracellular enzyme of T. denticola contains a single molecular species with a molecular mass of 59 kDa. Since it hydrolyses both HA and CS, it can more appropriately be termed a hyaluronoglucosaminidase (HGase). The HGase has been localized at the cell surface by electron microscopy and may play an active role in the degradation of connective tissue ground substance in the initiation and progression of periodontal disease.


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A. M. Edwards, H. F. Jenkinson, M. J. Woodward, and D. Dymock
Binding Properties and Adhesion-Mediating Regions of the Major Sheath Protein of Treponema denticola ATCC 35405
Infect. Immun., May 1, 2005; 73(5): 2891 - 2898.
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